| IED ID | IndEnz0002007849 |
| Enzyme Type ID | protease007849 |
| Protein Name |
PAN2-PAN3 deadenylation complex catalytic subunit PAN2 EC 3.1.13.4 Inactive ubiquitin carboxyl-terminal hydrolase 52 PAB1P-dependent poly A -specific ribonuclease Poly A -nuclease deadenylation complex subunit 2 PAN deadenylation complex subunit 2 |
| Gene Name | PAN2 KIAA0710 USP52 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNFEGLDPGLAEYAPAMHSALDPVLDAHLNPSLLQNVELDPEGVALEALPVQESVHIMEGVYSELHSVVAEVGVPVSVSHFDLHEEMLWVGSHGGHATSFFGPALERYSSFQVNGSDDIRQIQSLENGILFLTKNNLKYMARGGLIIFDYLLDENEDMHSLLLTDSSTLLVGGLQNHIIEIDLNTVQETQKYAVETPGVTIMRQTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVHGNLLAACGFSSRLTGLACDRFLKVYDLRMMRAITPLQVHVDPAFLRFIPTYTSRLAIISQSGQCQFCEPTGLANPADIFHVNPVGPLLMTFDVSASKQALAFGDSEGCVHLWTDSPEPSFNPYSRETEFALPCLVDSLPPLDWSQDLLPLSLIPVPLTTDTLLSDWPAANSAPAPRRAPPVDAEILRTMKKVGFIGYAPNPRTRLRNQIPYRLKESDSEFDSFSQVTESPVGREEEPHLHMVSKKYRKVTIKYSKLGLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHLCQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASALGLILADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQAYRGAGGSSFCSSGDSVIGQLFSCEMENCSLCRCGSETVRASSTLLFTLSYPDGSKSDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSKEADFWRMQAEVAFKMAVKKHGGEISKNKEFALADWKELGSPEGVLVCPSIEELKNVWLPFSIRMKMTKNKGLDVCNWTDGDEMQWGPARAEEEHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHQRKEGVTHQQWYLFNDFLIEPIDKHEAVQFDMNWKVPAILYYVKRNLNSRYNLNIKNPIEASVLLAEASLARKQRKTHTTFIPLMLNEMPQIGDLVGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKISSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETHDSIEDARTALQLYRKYLELSKNGTEPESFHKVLKGLYEKGRKMDWKVPEPEGQTSPKNAAVFSSVLAL |
| Enzyme Length | 1202 |
| Uniprot Accession Number | Q504Q3 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by the regulatory subunit PAN3. {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14583602}; |
| DNA Binding | |
| EC Number | 3.1.13.4 |
| Enzyme Function | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:16284618, ECO:0000269|PubMed:23398456}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Metal binding (4); Modified residue (2); Mutagenesis (1); Natural variant (3); Region (1); Repeat (4); Sequence conflict (2) |
| Keywords | Alternative splicing;Cytoplasm;Exonuclease;Hydrolase;Metal-binding;Nuclease;Nucleus;Phosphoprotein;Reference proteome;Repeat;WD repeat;mRNA processing |
| Interact With | Q58A45; Q9HCJ0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:16284618}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:18625844, ECO:0000269|PubMed:23398456}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:16284618}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:16284618}. |
| Modified Residue | MOD_RES 791; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 1189; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11283721; 14749774; 15475613; 16141059; 17245413; 17353931; 17595167; 19239894; 19615732; 19913121; 20628086; 20711500; 21981923; 29599486; 33097710; |
| Motif | |
| Gene Encoded By | |
| Mass | 135,368 |
| Kinetics | |
| Metal Binding | METAL 978; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 980; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1087; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1139; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182" |
| Rhea ID | |
| Cross Reference Brenda | 3.1.13.4; |